2drd
From Proteopedia
(New page: 200px<br /> <applet load="2drd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2drd, resolution 3.10Å" /> '''Crystal structure o...) |
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| - | [[Image:2drd.gif|left|200px]]<br /> | + | [[Image:2drd.gif|left|200px]]<br /><applet load="2drd" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2drd, resolution 3.10Å" /> | caption="2drd, resolution 3.10Å" /> | ||
'''Crystal structure of a multidrug transporter reveal a functionally rotating mechanism'''<br /> | '''Crystal structure of a multidrug transporter reveal a functionally rotating mechanism'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2DRD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MIY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2DRD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MIY:'>MIY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DRD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transporter]] | [[Category: transporter]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:22:08 2008'' |
Revision as of 15:22, 15 February 2008
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Crystal structure of a multidrug transporter reveal a functionally rotating mechanism
Overview
AcrB is a principal multidrug efflux transporter in Escherichia coli that, cooperates with an outer-membrane channel, TolC, and a membrane-fusion, protein, AcrA. Here we describe crystal structures of AcrB with and, without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the, three functional states of the transport cycle. Bound substrate was found, in the periplasmic domain of one of the three protomers. The voluminous, binding pocket is aromatic and allows multi-site binding. The structures, indicate that drugs are exported by a three-step functionally rotating, mechanism in which substrates undergo ordered binding change.
About this Structure
2DRD is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of a multidrug transporter reveal a functionally rotating mechanism., Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A, Nature. 2006 Sep 14;443(7108):173-9. Epub 2006 Aug 16. PMID:16915237
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